Second double-stranded RNA binding domain of dicer-like ribonuclease 1: structural and biochemical characterization.
Biochemistry
; 51(51): 10159-66, 2012 Dec 21.
Article
em En
| MEDLINE
| ID: mdl-23194006
ABSTRACT
Dicer-like ribonuclease III enzymes are involved in different paths related to RNA silencing in plants. Little is known about the structural aspects of these processes. Here we present a structural characterization of the second double-stranded RNA binding domain (dsRBD) of DCL1, which is presumed to participate in pri-micro-RNA recognition and subcellular localization of this protein. We determined the solution structure and found that it has a canonical fold but bears some variation with respect to other homologous domains. We also found that this domain binds both double-stranded RNA and double-stranded DNA, in contrast to most dsRBDs. Our characterization shows that this domain likely has functions other than substrate recognition and binding.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
RNA de Cadeia Dupla
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Proteínas de Ciclo Celular
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Proteínas de Arabidopsis
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Ribonuclease III
Idioma:
En
Ano de publicação:
2012
Tipo de documento:
Article